KEGG   ENZYME: 2.6.1.34
Entry
EC 2.6.1.34                 Enzyme                                 
Name
UDP-N-acetylbacillosamine transaminase;
uridine diphospho-4-amino-2-acetamido-2,4,6-trideoxyglucose aminotransferase;
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase;
UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase;
pglE (gene name);
UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose:2-oxoglutarate aminotransferase
Class
Transferases;
Transferring nitrogenous groups;
Transaminases
Sysname
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine:2-oxoglutarate aminotransferase
Reaction(IUBMB)
UDP-N-acetylbacillosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + L-glutamate [RN:R04529]
Reaction(KEGG)
R04529
Substrate
UDP-N-acetylbacillosamine [CPD:C04630];
2-oxoglutarate [CPD:C00026]
Product
UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose [CPD:C04613];
L-glutamate [CPD:C00025]
Comment
A pyridoxal-phosphate protein. The enzyme is involved in biosynthesis of UDP-N,N'-diacetylbacillosamine, an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species [2-4] and O-linked glycosylation of certain L-serine residues in Neisseria species [5].
History
EC 2.6.1.34 created 1972, modified 2013
Pathway
ec00520  Amino sugar and nucleotide sugar metabolism
ec00541  O-Antigen nucleotide sugar biosynthesis
ec01100  Metabolic pathways
Orthology
K15910  UDP-N-acetylbacillosamine transaminase
K24302  UDP-N-acetylbacillosamine transaminase
Genes
PHAGPZ638_20290
VCZVAB027_3604
VVUVV1_0810
VVYVV0310
VVMVVMO6_02806
VVLVV93_v1c03000
SSPAK0I31_07120
IABK5X84_02500
PSAZPA25_03950
ASEMNNL22_10255
TBOGLT988_19805
HAHHO5O45_03555
TVLFAZ95_31085
HWIA0Z60_01040
HPULNCTC13154_00066(btrR)
SULGFJR48_03870(pglE)
SMAXFJR03_06725(pglE)
SAQTGJV85_04760
CJECj1121c(pglE)
CJBBN148_1121c(pglE)
CJJCJJ81176_1139(pglE)
CJUC8J_1062(wlaK)
CJNICDCCJ07001_1077
CJICJSA_1063(pglE)
CJMCJM1_1100(pglE)
CJSCJS3_1168
CJPA911_05430
CJEJN564_01089
CJEUN565_01132
CJENN755_01125
CJEIN135_01158
CJERH730_06580
CJVMTVDSCj20_1125(pglE)
CJYQZ67_01198(pglE)
CJQUC78_1079(pglE)
CJLPJ17_05750
CJWPJ18_05560
CJRCJE1264(pglE)
CJDJJD26997_0599(pglE)
CJZM635_01310
CJXBN867_11130
CFFCFF8240_1355
CFTCFF04554_1371(pglE)
CFVCFVI03293_1394(pglE)
CFXCFV97608_1494(pglE)
CFZCSG_14940
CAMPCFT03427_1319(pglE)
CFPCR44_06675
CCVCCV52592_1203(pglE)
CHACHAB381_0950
CCOCCC13826_0448(pglE)
CCOCCCON33237_1461(pglE)
CLACLA_1257(pglE)
CLRUPTC16701_1240(pglE)
CLMUPTC16712_1258(pglE)
CLQUPTC4110_1242(pglE)
CLNUPTC3659_1477(pglE)
CLLCONCH_1208(pglE)
CCOLBN865_10070
CCCG157_03325
CCQN149_1063(pglE)
CCFYSQ_03360
CCYYSS_06075
CCOIYSU_03395
CCOFVC76_05505(pglE)
CCOOATE51_01360(pglE)
CAJCIG1485E_1366(pglE)
CISCINS_1222(pglE)
CVOCVOL_1236(pglE)
CPELCPEL_1363(pglE)
CAMRCAQ16704_1268(pglE)
CSMCSUB8521_1444(pglE)
CSFCSUB8523_1540(pglE)
CGRACGRAC_1486(pglE)
CURECUREO_1369(pglE)
CHYOCHH_1360(pglE)
CHVCHELV3228_0574(pglE)
CSPFCSF_1367(pglE)
CPINCPIN18020_1229(pglE)
CCUNCCUN_1175(pglE)
CLXCLAN_1156(pglE)
CAVICAV_0412(pglE)
CHWA2J15_001370
CAMZCVIC12175_0406(pglE)
CAMYCSUIS_1214(pglE)
COJCORN_1327(pglE)
CUXCUP3940_1113(pglE)
CRXCRECT_1672(pglE)
CGEOCGEO_1569(pglE)
CCORCCORG_0298(pglE)
CARMCARM_1290(pglE)
CMUCCMCT_0321(pglE)
CSHOCSHOW_1514(pglE)
CINFCINF_1315(pglE)
CNVCNZW441b_1125(pglE)
CVUCVULP_0516(pglE)
AFCAFAEC_1298
AHSAHALO_0835
AMYTAMYT_0891
AMARAMRN_0898
HBVABIV_0886
HCJHCR_14890(pglE)
SLHYH65_07060
SINUIMZ28_10310
CPAFC6V80_08595
FENJ0383_14240
NMFNMS_2738
RCLNYR17_09625
 » show all
Reference
1  [PMID:4381351]
  Authors
Distler J, Kaufman B, Roseman S.
  Title
Enzymic synthesis of a diamino sugar nucleotide by extracts of type XIV Diplococcus pneumoniae.
  Journal
Arch Biochem Biophys 116:466-78 (1966)
DOI:10.1016/0003-9861(66)90054-3
Reference
2  [PMID:17087520]
  Authors
Olivier NB, Chen MM, Behr JR, Imperiali B
  Title
In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system.
  Journal
Biochemistry 45:13659-69 (2006)
DOI:10.1021/bi061456h
Reference
3  [PMID:16286454]
  Authors
Schoenhofen IC, McNally DJ, Vinogradov E, Whitfield D, Young NM, Dick S, Wakarchuk WW, Brisson JR, Logan SM
  Title
Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways.
  Journal
J Biol Chem 281:723-32 (2006)
DOI:10.1074/jbc.M511021200
  Sequence
[cje:Cj1121c]
Reference
4  [PMID:18198901]
  Authors
Rangarajan ES, Ruane KM, Sulea T, Watson DC, Proteau A, Leclerc S, Cygler M, Matte A, Young NM
  Title
Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter  jejuni.
  Journal
Biochemistry 47:1827-36 (2008)
DOI:10.1021/bi702032r
Reference
5  [PMID:21542610]
  Authors
Hartley MD, Morrison MJ, Aas FE, Borud B, Koomey M, Imperiali B
  Title
Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N'-diacetylbacillosamine.
  Journal
Biochemistry 50:4936-48 (2011)
DOI:10.1021/bi2003372
Other DBs
ExplorEnz - The Enzyme Database: 2.6.1.34
IUBMB Enzyme Nomenclature: 2.6.1.34
ExPASy - ENZYME nomenclature database: 2.6.1.34
BRENDA, the Enzyme Database: 2.6.1.34
CAS: 37277-89-7

DBGET integrated database retrieval system